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PDBsum entry 1qpl

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
1qpl
Jmol
Contents
Protein chains
107 a.a. *
Ligands
587 ×2
Waters ×14
* Residue conservation analysis
HEADER    ISOMERASE                               25-MAY-99   1QPL
TITLE     FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (FK506-BINDING PROTEIN);
COMPND   3 CHAIN: A, C;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    IMMUNOPHILIN-DRUG COMPLEX, CIS-TRANS ISOMERASE, PEPTIDYL-
KEYWDS   2 PROLYL ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.W.BECKER,J.ROTONDA
REVDAT   3   24-FEB-09 1QPL    1       VERSN
REVDAT   2   28-JUN-00 1QPL    1       SOURCE
REVDAT   1   16-AUG-99 1QPL    0
JRNL        AUTH   J.W.BECKER,J.ROTONDA,J.G.CRYAN,M.MARTIN,
JRNL        AUTH 2 W.H.PARSONS,P.J.SINCLAIR,G.WIEDERRECHT,F.WONG
JRNL        TITL   32-INDOLYL ETHER DERIVATIVES OF ASCOMYCIN:
JRNL        TITL 2 THREE-DIMENSIONAL STRUCTURES OF COMPLEXES WITH
JRNL        TITL 3 FK506-BINDING PROTEIN.
JRNL        REF    J.MED.CHEM.                   V.  42  2798 1999
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   10425089
JRNL        DOI    10.1021/JM9806042
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   L.B.PETERSON,J. G.CRYAN,R.ROSA,M.M.MARTIN,
REMARK   1  AUTH 2 M.B.WILUSZ,P.J.SINCLAIR,F.WONG,J.N.PARSONS,
REMARK   1  AUTH 3 S.J.O'KEEFE,W.H.PARSONS,M.WYVRATT,N.H.SIGAL,
REMARK   1  AUTH 4 A.R.WILLIAMSON,G.J.WIEDERRECHT
REMARK   1  TITL   A TACROLIMUS-RELATED IMMUNOSUPPRESSANT WITH
REMARK   1  TITL 2 BIOCHEMICAL PROPERTIES DISTINCT FROM THOSE OF
REMARK   1  TITL 3 TACROLIMUS.
REMARK   1  REF    TRANSPLANTATION               V.  65    10 1998
REMARK   1  REFN                   ISSN 0041-1337
REMARK   1  DOI    10.1097/00007890-199801150-00004
REMARK   1 REFERENCE 2
REMARK   1  AUTH   F.J.DUMONT,S.KOPRAK,M. J.STARUCH,A.TALENTO,G.KOO,
REMARK   1  AUTH 2 C.DASILVA,P. J.SINCLAIR,F.WONG,J.WOODS,J.BARKER,
REMARK   1  AUTH 3 J.PIVNICHNY,I.SINGER,N. H.SIGAL,A. R.WILLIAMSON,
REMARK   1  AUTH 4 W. H.PARSONS,M WYVRATT
REMARK   1  TITL   A TACROLIMUS-RELATED IMMUNOSUPPRESSANT WITH
REMARK   1  TITL 2 REDUCED TOXICITY.
REMARK   1  REF    TRANSPLANTATION               V.  65    18 1998
REMARK   1  REFN                   ISSN 0041-1337
REMARK   1  DOI    10.1097/00007890-199801150-00005
REMARK   1 REFERENCE 3
REMARK   1  AUTH   P.J.SINCLAIR,F.WONG,M.J.STARUCH,G.WIEDERRECHT,
REMARK   1  AUTH 2 W.H.PARSONS,F.DUMONT,M.WYVRATT
REMARK   1  TITL   PREPARATION AND IN VITRO ACTIVITIES OF NAPHTHYL
REMARK   1  TITL 2 AND INDOLYL ETHER DERIVATIVES OF THE FK-506
REMARK   1  TITL 3 RELATED IMMUNOSUPPRESSIVE MACROLIDE ASCOMYCIN.
REMARK   1  REF    BIOORG.MED.CHEM.LETT.         V.   6  2193 1996
REMARK   1  REFN                   ISSN 0960-894X
REMARK   1  DOI    10.1016/0960-894X(96)00398-8
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.6
REMARK   3   NUMBER OF REFLECTIONS             : 8527
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : A POSTERIORI
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.223
REMARK   3   FREE R VALUE                     : 0.342
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 903
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.00
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 675
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370
REMARK   3   BIN FREE R VALUE                    : 0.3420
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 46
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.050
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1664
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 134
REMARK   3   SOLVENT ATOMS            : 14
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 68.48
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.40
REMARK   3   ESD FROM SIGMAA              (A) : 0.51
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.51
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.19
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1QPL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB009118.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-91
REMARK 200  TEMPERATURE           (KELVIN) : 298.0
REMARK 200  PH                             : 6.1
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HARVARD DATA COLLECTION
REMARK 200                                   SYSTEM FOR X-RAY AREA
REMARK 200                                   DETECTORS V. 2.0-03
REMARK 200  DATA SCALING SOFTWARE          : XENGEN, FBSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12979
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.330
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.1
REMARK 200  DATA REDUNDANCY                : 6.410
REMARK 200  R MERGE                    (I) : 0.05850
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 29.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61
REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: PROTEIN PORTION OF PDB ENTRY 1FKD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 69.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM
REMARK 280  PHOSPHATE, PH 6.1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.87000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       28.60500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.87000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       28.60500
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       59.87000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       28.60500
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       59.87000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       59.87000
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       28.60500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ARG A  18       96.80    -61.15
REMARK 500    ASP A  32       35.34    -79.10
REMARK 500    LYS A  34      118.49    -34.10
REMARK 500    SER A  38      114.27   -162.59
REMARK 500    ASN A  43       12.14     50.20
REMARK 500    ALA A  81     -116.58   -113.92
REMARK 500    TYR A  82       61.76   -116.60
REMARK 500    PRO A  88      120.52    -36.97
REMARK 500    ARG C 213      -55.65   -130.04
REMARK 500    ARG C 218      107.66    -54.87
REMARK 500    ASP C 232       30.00    -92.82
REMARK 500    GLN C 253       81.37    -56.75
REMARK 500    ALA C 281      -97.13   -115.00
REMARK 500    TYR C 282      -66.23   -123.51
REMARK 500    ALA C 284      -81.43    -54.82
REMARK 500    HIS C 287      107.38   -161.06
REMARK 500    PRO C 288      113.94    -39.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH C 414        DISTANCE =  6.80 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 587 A 108
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 587 C 308
DBREF  1QPL A    1   107  UNP    P62942   FKB1A_HUMAN      1    107
DBREF  1QPL C  201   307  UNP    P62942   FKB1A_HUMAN      1    107
SEQRES   1 A  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG
SEQRES   2 A  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR
SEQRES   3 A  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER
SEQRES   4 A  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS
SEQRES   5 A  107  GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN
SEQRES   6 A  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO
SEQRES   7 A  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE
SEQRES   8 A  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU
SEQRES   9 A  107  LYS LEU GLU
SEQRES   1 C  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG
SEQRES   2 C  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR
SEQRES   3 C  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER
SEQRES   4 C  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS
SEQRES   5 C  107  GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN
SEQRES   6 C  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO
SEQRES   7 C  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE
SEQRES   8 C  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU
SEQRES   9 C  107  LYS LEU GLU
HET    587  A 108      67
HET    587  C 308      67
HETNAM     587 C32-O-(1-METHYL-INDOL-5-YL) 18-HYDROXY-ASCOMYCIN
HETSYN     587 L-709,587
FORMUL   3  587    2(C52 H76 N2 O13)
FORMUL   5  HOH   *14(H2 O)
HELIX    1   1 ILE A   56  GLN A   65  1                                  10
HELIX    2   2 PRO A   78  ALA A   81  5                                   4
HELIX    3   3 SER C  239  ASN C  243  1                                   5
HELIX    4   4 ILE C  256  GLN C  265  1                                  10
HELIX    5   5 PRO C  278  ALA C  281  5                                   4
SHEET    1   A 5 VAL A   2  SER A   8  0
SHEET    2   A 5 ARG A  71  ILE A  76 -1  O  ARG A  71   N  ILE A   7
SHEET    3   A 5 LEU A  97  LEU A 106 -1  N  LEU A  97   O  ILE A  76
SHEET    4   A 5 THR A  21  LEU A  30 -1  O  MET A  29   N  VAL A  98
SHEET    5   A 5 LYS A  35  SER A  38 -1  N  PHE A  36   O  GLY A  28
SHEET    1  A1 5 VAL A   2  SER A   8  0
SHEET    2  A1 5 ARG A  71  ILE A  76 -1  O  ARG A  71   N  ILE A   7
SHEET    3  A1 5 LEU A  97  LEU A 106 -1  N  LEU A  97   O  ILE A  76
SHEET    4  A1 5 THR A  21  LEU A  30 -1  O  MET A  29   N  VAL A  98
SHEET    5  A1 5 PHE A  46  MET A  49 -1  O  PHE A  46   N  VAL A  24
SHEET    1   B 5 VAL C 202  SER C 208  0
SHEET    2   B 5 ARG C 271  ILE C 276 -1  O  ARG C 271   N  ILE C 207
SHEET    3   B 5 LEU C 297  LEU C 306 -1  O  LEU C 297   N  ILE C 276
SHEET    4   B 5 THR C 221  LEU C 230 -1  O  MET C 229   N  VAL C 298
SHEET    5   B 5 LYS C 235  SER C 238 -1  N  PHE C 236   O  GLY C 228
SHEET    1  B1 5 VAL C 202  SER C 208  0
SHEET    2  B1 5 ARG C 271  ILE C 276 -1  O  ARG C 271   N  ILE C 207
SHEET    3  B1 5 LEU C 297  LEU C 306 -1  O  LEU C 297   N  ILE C 276
SHEET    4  B1 5 THR C 221  LEU C 230 -1  O  MET C 229   N  VAL C 298
SHEET    5  B1 5 PHE C 246  MET C 249 -1  O  PHE C 246   N  VAL C 224
SITE     1 AC1 18 TYR A  26  PHE A  36  ASP A  37  ARG A  42
SITE     2 AC1 18 PHE A  46  GLU A  54  VAL A  55  ILE A  56
SITE     3 AC1 18 TRP A  59  ALA A  81  TYR A  82  ILE A  91
SITE     4 AC1 18 PHE A  99  ILE C 207  SER C 208  GLN C 253
SITE     5 AC1 18 HIS C 287  587 C 308
SITE     1 AC2 14 GLN A  53  GLU A  54  VAL A  55  587 A 108
SITE     2 AC2 14 THR C 206  TYR C 226  ASP C 237  PHE C 246
SITE     3 AC2 14 GLU C 254  VAL C 255  ILE C 256  TRP C 259
SITE     4 AC2 14 ALA C 281  TYR C 282
CRYST1  119.740  119.740   57.210  90.00  90.00  90.00 I 4          16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008351  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008351  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017479        0.00000
      
PROCHECK
Go to PROCHECK summary
 References